ID N9F635_ACIHA Unreviewed; 679 AA.
AC N9F635;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=ATP-dependent DNA helicase Rep {ECO:0000256|HAMAP-Rule:MF_01920};
DE EC=5.6.2.4 {ECO:0000256|HAMAP-Rule:MF_01920};
DE AltName: Full=DNA 3'-5' helicase Rep {ECO:0000256|HAMAP-Rule:MF_01920};
GN Name=rep {ECO:0000256|HAMAP-Rule:MF_01920};
GN ORFNames=F927_01742 {ECO:0000313|EMBL:ENW18298.1};
OS Acinetobacter haemolyticus CIP 64.3 = MTCC 9819.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217659 {ECO:0000313|EMBL:ENW18298.1, ECO:0000313|Proteomes:UP000017667};
RN [1] {ECO:0000313|EMBL:ENW18298.1, ECO:0000313|Proteomes:UP000017667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 64.3 {ECO:0000313|EMBL:ENW18298.1,
RC ECO:0000313|Proteomes:UP000017667};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter haemolyticus CIP 64.3.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Rep helicase is a single-stranded DNA-dependent ATPase
CC involved in DNA replication; it can initiate unwinding at a nick in the
CC DNA. It binds to the single-stranded DNA and acts in a progressive
CC fashion along the DNA in the 3' to 5' direction. {ECO:0000256|HAMAP-
CC Rule:MF_01920}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618, ECO:0000256|HAMAP-
CC Rule:MF_01920};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01920};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01920}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922, ECO:0000256|HAMAP-Rule:MF_01920}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ENW18298.1}.
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DR EMBL; APQQ01000020; ENW18298.1; -; Genomic_DNA.
DR RefSeq; WP_004638202.1; NZ_KB849800.1.
DR AlphaFoldDB; N9F635; -.
DR GeneID; 56329936; -.
DR PATRIC; fig|1217659.3.peg.1706; -.
DR HOGENOM; CLU_004585_5_2_6; -.
DR Proteomes; UP000017667; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01920; Helicase_Rep; 1.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR005752; Helicase_Rep.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR NCBIfam; TIGR01074; rep; 1.
DR PANTHER; PTHR11070:SF64; ATP-DEPENDENT DNA HELICASE REP; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01920};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_01920}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_01920};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01920};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01920};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01920};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01920}.
FT DOMAIN 5..287
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 288..571
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT BINDING 285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01920"
SQ SEQUENCE 679 AA; 77659 MW; 32FFB8D3A6A5FEA2 CRC64;
MSSASQLNDK QLEAMKYVQG PLLVLAGAGS GKTSVITRKI AFLVQQCGIP AYRITAMTFT
NKAAREMKER VGKLLSREEA KGLSVSTFHT FGLNLLRLEL KNLPLKANFS ILDADDCKRI
LMDLMQRDNM SGAESKELIA KAMKKISDWK NDLILPEQAH STCETVEDVQ LAHLYQLYER
NLRAYNAVDF DDLIVMPTRL LQENAEVRDK WQNRVRYLLV DEYQDTNTAQ YTLVKLLVGV
MGQFTAVGDD DQSIYAWRGA KPENMALLKD DFHNLKVIKL EQNYRSTSRI LKAANAVIEN
NPHIFDKKLW SDKGHGENIR VITCLNDDDE AERVVKDLIT HKLMNGKNWK DYAILYRGNF
QARVLETQLR QMQIPYKLSG GQSFFARAEI KDVMSYLRLI INPEDDSAFL RIINTPKRAI
GPVTLEKLGL FAQENTLSLL TASSDQRLSM VLPKKAATQL HEFADFIATF TRELLDDDEP
VPKVRQMINE AGYIDYVREQ AATPAQEKTK IDNIESLYTS IQNLINRTDD VDEKNIESVI
RKLVLLDMLE QQQEEEDTDK VNLLTLHAAK GLEFPYVYMI GLEEELLPHK NSIASETIEE
ERRLMYVGIT RARQGLTLTL AEQRKNGGQM RQMTPSRFLD ELPQDDLEWH GRKKKLAPNV
DPKEQAQQYL ANLKALLKR
//
